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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR048952",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF20917": "Asparaginal-tRNA synthetase, N-terminal domain"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR048952",
"name": "Asparagine--tRNA ligase, N-terminal domain",
"type": "Domain",
"children": []
},
"name": {
"name": "Asparagine--tRNA ligase, N-terminal domain",
"short": "AsnRS_N"
},
"description": [
{
"text": "<p>This domain is found at the N-terminal domain of the eukaryotic cytoplasmic protein Asparagine--tRNA ligase (AsnRS, also known as NARS1). AsnRS is essential for protein translation and has been related to autoimmune and neurological diseases. Unlike its bacterial homologues, this protein has a conserved N-terminal extension, represented in this entry, connected by an unstructured tether to the part of the enzyme that has homologues within eukaryotes and prokaryotes: an anticodon-binding domain ([interpro:IPR004365]), a hinge region (HR), and a catalytic domain ([interpro:IPR004364]).</p>\n\n<p>This domain folds into two α-helices and three β-strands that form a parallel/antiparallel mixed β-sheet and has a characteristic lysine-rich helical motif that interacts with tRNA. It also shows chemokine activity through its interaction with C-C chemokine receptor 3 (CCR3) and the promotion of NRS-CCR3-mediated proinflammatory signalling [[cite:PUB00054624], [cite:PUB00152072], [cite:PUB00152073]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00054624": {
"PMID": 21134380,
"ISBN": null,
"volume": "405",
"issue": "4",
"year": 2011,
"title": "A hybrid structural model of the complete Brugia malayi cytoplasmic asparaginyl-tRNA synthetase.",
"URL": null,
"raw_pages": "1056-69",
"medline_journal": "J Mol Biol",
"ISO_journal": "J. Mol. Biol.",
"authors": [
"Crepin T",
"Peterson F",
"Haertlein M",
"Jensen D",
"Wang C",
"Cusack S",
"Kron M."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.jmb.2010.11.049"
},
"PUB00152073": {
"PMID": 32738225,
"ISBN": null,
"volume": "107",
"issue": "2",
"year": 2020,
"title": "De Novo and Bi-allelic Pathogenic Variants in NARS1 Cause Neurodevelopmental Delay Due to Toxic Gain-of-Function and Partial Loss-of-Function Effects.",
"URL": null,
"raw_pages": "311-324",
"medline_journal": "Am J Hum Genet",
"ISO_journal": "Am J Hum Genet",
"authors": [
"Manole A",
"Efthymiou S",
"O'Connor E",
"Mendes MI",
"Jennings M",
"Maroofian R",
"Davagnanam I",
"Mankad K",
"Lopez MR",
"Salpietro V",
"Harripaul R",
"Badalato L",
"Walia J",
"Francklyn CS",
"Athanasiou-Fragkouli A",
"Sullivan R",
"Desai S",
"Baranano K",
"Zafar F",
"Rana N",
"Ilyas M",
"Horga A",
"Kara M",
"Mattioli F",
"Goldenberg A",
"Griffin H",
"Piton A",
"Henderson LB",
"Kara B",
"Aslanger AD",
"Raaphorst J",
"Pfundt R",
"Portier R",
"Shinawi M",
"Kirby A",
"Christensen KM",
"Wang L",
"Rosti RO",
"Paracha SA",
"Sarwar MT",
"Jenkins D; SYNAPS Study Group",
"Ahmed J",
"Santoni FA",
"Ranza E",
"Iwaszkiewicz J",
"Cytrynbaum C",
"Weksberg R",
"Wentzensen IM",
"Guillen Sacoto MJ",
"Si Y",
"Telegrafi A",
"Andrews MV",
"Baldridge D",
"Gabriel H",
"Mohr J",
"Oehl-Jaschkowitz B",
"Debard S",
"Senger B",
"Fischer F",
"van Ravenwaaij C",
"Fock AJM",
"Stevens SJC",
"Bahler J",
"Nasar A",
"Mantovani JF",
"Manzur A",
"Sarkozy A",
"Smith DEC",
"Salomons GS",
"Ahmed ZM",
"Riazuddin S",
"Riazuddin S",
"Usmani MA",
"Seibt A",
"Ansar M",
"Antonarakis SE",
"Vincent JB",
"Ayub M",
"Grimmel M",
"Jelsig AM",
"Hjortshoj TD",
"Karstensen HG",
"Hummel M",
"Haack TB",
"Jamshidi Y",
"Distelmaier F",
"Horvath R",
"Gleeson JG",
"Becker H",
"Mandel JL",
"Koolen DA",
"Houlden H."
],
"DOI_URL": "https://doi.org/10.1016/j.ajhg.2020.06.016"
},
"PUB00152072": {
"PMID": 30171954,
"ISBN": null,
"volume": "120",
"issue": "Pt A",
"year": 2018,
"title": "Unique N-terminal extension domain of human asparaginyl-tRNA synthetase elicits CCR3-mediated chemokine activity.",
"URL": null,
"raw_pages": "835-845",
"medline_journal": "Int J Biol Macromol",
"ISO_journal": "Int J Biol Macromol",
"authors": [
"Park JS",
"Park MC",
"Lee KY",
"Goughnour PC",
"Jeong SJ",
"Kim HS",
"Kim HJ",
"Lee BJ",
"Kim S",
"Han BW."
],
"DOI_URL": "https://doi.org/10.1016/j.ijbiomac.2018.08.171"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 61,
"interactions": 0,
"matches": 3990,
"pathways": 1,
"proteins": 3977,
"proteomes": 2593,
"sets": 0,
"structural_models": {
"alphafold": 3620,
"bfvd": 0
},
"structures": 5,
"taxa": 7259
},
"entry_annotations": {
"alignment:seed": 203,
"alignment:full": 2742
},
"cross_references": {
"ec": {
"displayName": "ENZYME",
"description": "ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.",
"rank": 19,
"accessions": [
{
"accession": "6.1.1.22",
"url": "https://enzyme.expasy.org/EC/6.1.1.22"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "4zya",
"name": "The N-terminal extension domain of human asparaginyl-tRNA synthetase"
}
}
}
